title: The effects of solution structure on the surface conformation and orientation of a cysteine-terminated antimicrobial peptide cecropin P1.
abstract: The surface structure of an antimicrobial peptide, cecropin P1, immobilized to a gold surface via a terminal cysteine residue was investigated. Using reflection-absorption infrared spectroscopy, surface plasmon resonance, and X-ray photoelectron spectroscopy, the effects of pH, solution conformation, and concentration on the immobilized peptide conformation, average orientation, and surface density were determined. Under all conditions investigated, the immobilized peptides were alpha-helical in a predominately flat, random orientation. The addition of the reducing agent Tris(2-carboxyethyl) phosphine hydrochloride to the buffer resulted in a twofold increase in immobilized peptide surface density.
authors.affiliation: Virginia Tech Department of Chemistry, Blacksburg, VA 24061, USA.
authors.forename: Joshua R
authors.initials: JR
authors.lastname: Uzarski
authors.forename: Abla
authors.initials: A
authors.lastname: Tannous
authors.forename: John R
authors.initials: JR
authors.lastname: Morris
authors.forename: Charlene M
authors.initials: CM
authors.lastname: Mello
mesh_terms: D000890:Anti-Infective Agents / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*; D019999:Pharmaceutical Solutions / Q000737:chemistry*; D013057:Spectrum Analysis; D020349:Surface Plasmon Resonance; D014965:X-Rays
chemical_list: D000890:Anti-Infective Agents; D010455:Peptides; D019999:Pharmaceutical Solutions; D003545:Cysteine; C070016:cecropin P1-LI